BACKGROUND: Pentraxins are a family of plasma proteins characterized by their pentameric assembly and calcium-dependent ligand binding. The recent determination of the crystal structure for a member of this family, human serum amyloid P component (SAP), provides a basis for the comparative analysis of the pentraxin family. RESULTS: We have compared the sequences, tertiary structures and quaternary arrangements of SAP with human C-reactive protein (CRP), Syrian hamster SAP (HSAP) and Limulus polyphemus CRP (LIM). These proteins can adopt a beta-jelly roll topology and a hydrophobic core similar to that seen in SAP. Only minor differences are observed in the positions of residues involved in coordinating calcium ions. CONCLUSIONS: Calcium-mediated ligand binding by CRP, HSAP and LIM is similar to that defined by the crystal structure of SAP, but sequence differences in the hydrophobic pocket explain the differential ligand specificities exhibited by the homologous proteins. Differences elsewhere, including insertions and deletions, account for the different (hexameric) quaternary structure of LIM.
BACKGROUND: Pentraxins are a family of plasma proteins characterized by their pentameric assembly and calcium-dependent ligand binding. The recent determination of the crystal structure for a member of this family, humanserum amyloid P component (SAP), provides a basis for the comparative analysis of the pentraxin family. RESULTS: We have compared the sequences, tertiary structures and quaternary arrangements of SAP with humanC-reactive protein (CRP), Syrian hamsterSAP (HSAP) and Limulus polyphemus CRP (LIM). These proteins can adopt a beta-jelly roll topology and a hydrophobic core similar to that seen in SAP. Only minor differences are observed in the positions of residues involved in coordinating calcium ions. CONCLUSIONS:Calcium-mediated ligand binding by CRP, HSAP and LIM is similar to that defined by the crystal structure of SAP, but sequence differences in the hydrophobic pocket explain the differential ligand specificities exhibited by the homologous proteins. Differences elsewhere, including insertions and deletions, account for the different (hexameric) quaternary structure of LIM.
Authors: Sanjay K Singh; Avinash Thirumalai; David J Hammond; Michael K Pangburn; Vinod K Mishra; David A Johnson; Antonio E Rusiñol; Alok Agrawal Journal: J Biol Chem Date: 2011-12-09 Impact factor: 5.157
Authors: Jason Y Y Wong; Bryan A Bassig; Wei Hu; Wei Jie Seow; Meredith S Shiels; Bu-Tian Ji; George S Downward; Yunchao Huang; Kaiyun Yang; Jihua Li; Jun He; Ying Chen; Allan Hildesheim; Roel Vermeulen; Qing Lan; Nathaniel Rothman Journal: J Toxicol Environ Health A Date: 2019-05-13
Authors: David J Hammond; Sanjay K Singh; James A Thompson; Bradley W Beeler; Antonio E Rusiñol; Michael K Pangburn; Lawrence A Potempa; Alok Agrawal Journal: J Biol Chem Date: 2010-09-14 Impact factor: 5.157
Authors: Laura Cruciani; Roberto Romero; Edi Vaisbuch; Juan Pedro Kusanovic; Tinnakorn Chaiworapongsa; Shali Mazaki-Tovi; Pooja Mittal; Giovanna Ogge; Francesca Gotsch; Offer Erez; Sun Kwon Kim; Zhong Dong; Percy Pacora; Ronald F Lamont; Lami Yeo; Sonia S Hassan; Gian Carlo Di Renzo Journal: J Perinat Med Date: 2010-03 Impact factor: 1.901